A novel method is proposed for obtaining Raman spectra from proteins in solution. Unlike resonance Raman techniques, which in general involve colored substances, the present technique works for colorless proteins, such as papain, or for metalloenzymes, such as carboxypeptidase. The method involves filling a long, hollow, fused quartz or Teflon optical fiber with a protein dissolved in a high refractive index solvent. The liquid-filled optical fiber then constitutes the sample, the Raman cell, and the entrance "slit" of a special Raman spectrometer. Because essentially all of the forward scattered Raman radiation is collected from 10 to 25 meters of fiber by total internal reflection, the Raman radiation is enhanced about 1000 times, compared to oridinary Raman cell techniques. This allows dilute solutions of proteins to be studied. The proposed method should allow for studies of the S-H vibrations of papain which are important, in catalytic activity, and for studies of Zn...O interactions in carboxypeptidase, which are also important because colorless metallocations are hard to study by other techniques.